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Activation of plasminogen by streptokinase is a species-specific event

机译：链激酶激活纤溶酶原是种特异性事件

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摘要

Streptokinase, one of the major blood-clot-dissolving agents, catalyzes the conversion of the plasma-zymogen (plasminogen) to the serine protease plasmin. Streptokinase genes fromtwo different S. equisimilis strains, isolated from equine and human, were cloned and expressed in Escherichia coli. Cloned streptokinase genes were investigated for their expression in E. coli by Western blot analysis and radial caseinolysis assay. Recombinant genes of streptokinase genes were similar to their native counterparts in terms of their molecular masses and exhibited preferential plasminogen activity. PAGE and Radial caseinolysis studies demonstrated that streptokinases secreted by streptococci from different hosts were able to differentially activate only the plasminogen derived fromthe same host. Streptokinase-plasminogen interaction indicated that human and equine plasminogens were cleaved at the same highly conserved site and an altered form of streptokinase was produced. This work strongly supports the idea that these streptokinases must share a common plasminogen binding domain and species-specific activation of plasminogen by streptokinases which reflecting the origin of the streptococcal isolate and the role of the streptokinase in the pathogenesis of streptococcal infections.
机译：链激酶是主要的血凝块溶解剂之一，可催化血浆酶原（纤溶酶原）向丝氨酸蛋白酶纤溶酶的转化。从马和人分离的两种不同的马链球菌菌株的链激酶基因被克隆并在大肠杆菌中表达。通过蛋白质印迹分析和放射状酪蛋白水解试验研究了克隆的链激酶基因在大肠杆菌中的表达。链激酶基因的重组基因在分子量方面类似于其天然对应物，并且表现出优先的纤溶酶原活性。 PAGE和径向酪蛋白水解研究表明，不同宿主的链球菌分泌的链激酶可以仅激活同一宿主的纤溶酶原。链激酶与纤溶酶原的相互作用表明，人和马​​纤溶酶原在同一高度保守的位点被切割，产生了链激酶的一种改变形式。这项工作强烈支持以下观点：这些链激酶必须共享一个共同的纤溶酶原结合域和链激酶的物种特异性纤溶酶原激活作用，这反映了链球菌分离株的起源以及链激酶在链球菌感染发病机理中的作用。

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